Two aromatic residues regulate the response of the human oxytocin receptor to the partial agonist arginine vasopressin

FEBS Lett. 1996 Nov 18;397(2-3):201-6. doi: 10.1016/s0014-5793(96)01135-0.


We investigated the mechanisms that regulate the efficacy of agonists in the arginine-vasopressin (AVP)/oxytocin (OT) receptor system. In this paper, we present evidence that AVP, a full agonist of the vasopressin receptors, acts as a partial agonist on the oxytocin receptor. We also found that AVP becomes a full agonist when two aromatic residues of the oxytocin receptor are replaced by the residues present at equivalent positions in the vasopressin receptor subtypes. Our results indicate that these two residues modulate the response of the oxytocin receptor to the partial agonist AVP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine Vasopressin / metabolism
  • Arginine Vasopressin / pharmacology*
  • Cell Line
  • Cloning, Molecular
  • Computer Simulation
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Oxytocin / analogs & derivatives
  • Oxytocin / metabolism
  • Oxytocin / pharmacology
  • Receptors, Oxytocin / agonists*
  • Receptors, Oxytocin / chemistry*
  • Receptors, Oxytocin / genetics
  • Receptors, Oxytocin / metabolism
  • Vasotocin / metabolism


  • Receptors, Oxytocin
  • Arginine Vasopressin
  • Oxytocin
  • oxytocin, Thr(4)-Gly(7)-
  • oxypressin
  • Vasotocin